2G5B
Crystal Structure of the anti-Bax monoclonal antibody 6A7 and a Bax peptide.
Summary for 2G5B
| Entry DOI | 10.2210/pdb2g5b/pdb |
| Descriptor | 6A7 Fab Light Chain, 6A7 Fab Heavy Chain, Bax Peptide, ... (8 entities in total) |
| Functional Keywords | 6a7, bax, fab, antibody, fab-peptide complex, apoptosis |
| Biological source | Mus musculus (house mouse) More |
| Total number of polymer chains | 12 |
| Total formula weight | 197961.31 |
| Authors | Peyerl, F.W.,Dai, S.,Murphy, G.A.,Marrack, P.,Kappler, J.W. (deposition date: 2006-02-22, release date: 2006-07-25, Last modification date: 2024-11-06) |
| Primary citation | Peyerl, F.W.,Dai, S.,Murphy, G.A.,Crawford, F.,White, J.,Marrack, P.,Kappler, J.W. Elucidation of some Bax conformational changes through crystallization of an antibody-peptide complex. Cell Death Differ., 14:447-452, 2007 Cited by PubMed Abstract: The Bcl-2 family member Bax plays a critical role in apoptosis. In healthy resting cells, Bax resides in the cytoplasm and loosely attached to the mitochondrial membrane. Apoptotic stimuli induce Bax activation, which is characterized by translocation and multimerization on the mitochondrial membrane surface resulting in exposure of an amino terminal epitope recognized by the monoclonal antibody 6A7. To understand the structural changes that occur during Bax activation, we determined the crystal structure of a Bax peptide bound to the 6A7 Fab fragment to a resolution of 2.3 A. The structure reveals the conformation of the 6A7 peptide epitope on Bax in the activated form and elucidates the extensive structural changes that Bax must undergo during the conversion from its native to its activated conformation. PubMed: 16946732DOI: 10.1038/sj.cdd.4402025 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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